F
IPR001328

Peptidyl-tRNA hydrolase

InterPro entry
Short namePept_tRNA_hydro
Overlapping
homologous
superfamilies
 
family relationships

Description

Peptidyl-tRNA hydrolase (
3.1.1.29
) (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis
[1, 2]
. Bacterial PTH has been found to be evolutionary related to a yeast protein
[3]
. This enzyme is interesting as a potential target for the discovery of new antimicrobial agents as it is critical for the viability of bacteria
[cite:PUB00106491]
}. It folds into a single α/β globular domain with seven β-strands forming a twisted mixed central β-sheet, surrounded by a total of six helices
[7]
.

This group also contains chloroplast RNA splicing 2 (CRS2), which is closely related nuclear-encoded protein required for the splicing of nine group II introns in chloroplasts
[6, 4, 5]
.

References

1.Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis. Garcia-Villegas MR, De La Vega FM, Galindo JM, Segura M, Buckingham RH, Guarneros G. EMBO J. 10, 3549-55, (1991). View articlePMID: 1833189

2.Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of Escherichia coli. De La Vega FM, Galindo JM, Old IG, Guarneros G. Gene 169, 97-100, (1996). View articlePMID: 8635758

3.New protein functions in yeast chromosome VIII. Ouzounis C, Bork P, Casari G, Sander C. Protein Sci. 4, 2424-8, (1995). View articlePMID: 8563640

4.Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S. EMBO J. 16, 4760-9, (1997). View articlePMID: 9303320

5.Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase. Goodall JJ, Chen GJ, Page MG. Biochemistry 43, 4583-91, (2004). View articlePMID: 15078105

6.Group II intron splicing factors derived by diversification of an ancient RNA-binding domain. Ostheimer GJ, Williams-Carrier R, Belcher S, Osborne E, Gierke J, Barkan A. EMBO J. 22, 3919-29, (2003). View articlePMID: 12881426

7.Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase. Ito K, Murakami R, Mochizuki M, Qi H, Shimizu Y, Miura KI, Ueda T, Uchiumi T. Nucleic Acids Res. (2012). PMID: 22923517

8.Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 A resolution. Zhang F, Song Y, Niu L, Teng M, Li X. Acta Biochim Biophys Sin (Shanghai) 47, 1005-10, (2015). PMID: 26508479

GO terms

biological process

  • None

cellular component

  • None

Cross References

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